Effect of Various ions on Atp Determinations Using the “Luciferine-Luciferase” System
- 1 January 1976
- journal article
- research article
- Published by Taylor & Francis in Archives Internationales de Physiologie et de Biochimie
- Vol. 84 (4) , 807-817
- https://doi.org/10.3109/13813457609067056
Abstract
(6 figures) Various salts and buffers used in routine as part of the ATP extraction procedures induce an important inhibition of the peak light emission produced by the “luciferine-luciferase” system. The nature of the anion is more important in determining the inhibitory effect than the nature of the cation. The series obtained when placing the anions studied by order of increasing effectiveness is as follows Ac−C1−I−C104−. KCIO4 appears thus as a strong inhibitor of the enzyme activity. It appears moreover to act competitively with respect to ATP, one mole of inhibitor binding per mole of ATP active site. These results are discussed in connection with the use of the “luciferine-luciferase” system for ATP and other energy-rich compounds' concentration measurements.This publication has 22 references indexed in Scilit:
- Analysis of adenine nucleotides at the picomole level with 32P-phosphoenolpyruvate and pyruvate kinaseAnalytical Biochemistry, 1975
- A facile radiometric technique for measuring ATPAnalytical Biochemistry, 1974
- Studies on the effect of nacl on the activity of Eriocheir sinensis glutamate dehydrogenaseInternational Journal of Biochemistry, 1974
- Effects of various ions on the succinic dehydrogenase activity of MytilusLife Sciences, 1971
- Effect of ions on sarcoplasmic reticulum fragmentsArchives of Biochemistry and Biophysics, 1968
- The Effect of Concentrated Salt Solutions on the Activity Coefficient of Acetyltetraglycine Ethyl EsterJournal of the American Chemical Society, 1965
- Inhibition of Acetoacetic Decarboxylase by AnionsJournal of Biological Chemistry, 1963
- Glutamate-dehydrogenase inactivation by reduced nicotinamide-adenine dinucleotide phosphateBiochemical Journal, 1962
- Interaction of myosin A with ionsArchives of Biochemistry and Biophysics, 1961
- The relationship of quaternary ammonium salts to the anionic sites of true and pseudo cholinesteraseBiochemical Journal, 1954